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Literature summary for 1.3.98.3 extracted from

  • Layer, G.; Heinz, D.W.; Jahn, D.; Schubert, W.D.
    Structure and function of radical SAM enzymes (2004), Curr. Opin. Chem. Biol., 8, 468-476.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
coproporphyrinogen-III + S-adenosyl-L-methionine Escherichia coli HemN catalyzes the prepenultimate step in anaerobic heme biosynthesis protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Reaction

Reaction Comment Organism Reaction ID
coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine this enzyme differs from EC 1.3.3.3, coproporphyrinogen oxidase, by using S-adenosyl-L-methionine, AdoMet, instead of oxygen as oxidant, it occurs mainly in bacteria, whereas eukaryotes use the oxygen-dependent oxidase, the reaction starts by using an electron from the reduced form of the enzyme’s [4Fe-4S] cluster to split AdoMet into methionine and the radical 5’-deoxyadenosin-5’-yl, this radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups. The conversion of –.CH-CH2-COO- leading to –CH=CH2 + CO2 + e- replaces the electron initially used, reaction mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
coproporphyrinogen-III + S-adenosyl-L-methionine HemN catalyzes the prepenultimate step in anaerobic heme biosynthesis Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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?
coproporphyrinogen-III + S-adenosyl-L-methionine HemN requires the juxtaposition of the [4Fe-4S] cluster and the cosubstrate S-adenosyl-L-methionine. The reaction involves the stereospecific hydrogen abstraction of the pro-S hydrogen from the propionate side chain beta-C of coproporphyrinogen-III, involvement of a coproporphyrinogenyl III radical, which is then decarboxylated releasing CO2 and forming the vinyl group, enzyme structure, two-domain enzyme consisting of the catalytic N- and an alpha-helical C-terminal domain, substrate binding mode Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
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Subunits

Subunits Comment Organism
monomer
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Escherichia coli

Synonyms

Synonyms Comment Organism
Coprogen oxidase
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Escherichia coli
coproporphyrinogen III oxidase
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Escherichia coli
coproporphyrinogen oxidase
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Escherichia coli
coproporphyrinogenase
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Escherichia coli
HemN
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Escherichia coli
More member of the Radical SAM protein family Escherichia coli
oxidase, coproporphyrinogen
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Escherichia coli
oxygen-independent coproporphyrinogen-III oxidase
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Escherichia coli
radical SAM enzyme
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center structure, location and coordination of the cofactor, HemN requires the juxtaposition of the [4Fe-4S] cluster and the cosubstrate S-adenosyl-L-methionine Escherichia coli